Marcin Jaciuk, David Scherf, Karol Kaszuba, Monika Gaik, Alexander Rau, Anna Kościelniak, Rościsław Krutyhołowa, Michał Rawski, Paulina Indyka, Andrea Graziadei, Andrzej Chramiec-Głąbik, Anna Biela, Dominika Dobosz, Ting-Yu Lin, Nour-el-Hana Abbassi, Alexander Hammermeister, Juri Rappsilber, Jan Kosinski, Raffael Schaffrath, Sebastian Glatt
Nucleic Acids Research, gkac1232, https://doi.org/10.1093/nar/gkac1232
The multi-subunit Elongator complex mediates the addition of a carboxymethyl group to wobble uridines in eukaryotic tRNAs. This tRNA modification is crucial to preserve the integrity of cellular proteomes and to protects us against severe neurodegenerative diseases. Elongator is organized in two distinct modules (i) the larger Elp123 subcomplex that binds and modifies the suitable tRNA substrate and (ii) the smaller Elp456 subcomplex that assists the release of the modified tRNA. The presented cryo-EM structures of Elongator show that the assemblies are very dynamic and undergo conformational rearrangements at consecutive steps of the process. Last but not least, the study provides a detailed reaction scheme and shows that the architecture of Elongator is highly conserved from yeast to mammals.